Dominant negative alleles of SEC10 reveal distinct domains involved in secretion and morphogenesis in yeast
The accurate targeting of secretory vesicles to distinct sites on the plasma membrane is necessary to achieve polarized growth and to establish specialized domains at the surface of eukaryotic cells. Members of a protein complex required for exocytosis, the exocyst, have been localized to regions of...
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Published in | Molecular biology of the cell Vol. 9; no. 7; pp. 1725 - 1739 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
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The American Society for Cell Biology
01.07.1998
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Abstract | The accurate targeting of secretory vesicles to distinct sites on the plasma membrane is necessary to achieve polarized growth and to establish specialized domains at the surface of eukaryotic cells. Members of a protein complex required for exocytosis, the exocyst, have been localized to regions of active secretion in the budding yeast Saccharomyces cerevisiae where they may function to specify sites on the plasma membrane for vesicle docking and fusion. In this study we have addressed the function of one member of the exocyst complex, Sec10p. We have identified two functional domains of Sec10p that act in a dominant-negative manner to inhibit cell growth upon overexpression. Phenotypic and biochemical analysis of the dominant-negative mutants points to a bifunctional role for Sec10p. One domain, consisting of the amino-terminal two-thirds of Sec10p directly interacts with Sec15p, another exocyst component. Overexpression of this domain displaces the full-length Sec10 from the exocyst complex, resulting in a block in exocytosis and an accumulation of secretory vesicles. The carboxy-terminal domain of Sec10p does not interact with other members of the exocyst complex and expression of this domain does not cause a secretory defect. Rather, this mutant results in the formation of elongated cells, suggesting that the second domain of Sec10p is required for morphogenesis, perhaps regulating the reorientation of the secretory pathway from the tip of the emerging daughter cell toward the mother-daughter connection during cell cycle progression. |
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AbstractList | The accurate targeting of secretory vesicles to distinct sites on
the plasma membrane is necessary to achieve polarized growth and to
establish specialized domains at the surface of eukaryotic cells.
Members of a protein complex required for exocytosis, the exocyst, have
been localized to regions of active secretion in the budding yeast
Saccharomyces cerevisiae
where they may function to
specify sites on the plasma membrane for vesicle docking and fusion. In
this study we have addressed the function of one member of the exocyst
complex, Sec10p. We have identified two functional domains of Sec10p
that act in a dominant-negative manner to inhibit cell growth upon
overexpression. Phenotypic and biochemical analysis of the
dominant-negative mutants points to a bifunctional role for Sec10p. One
domain, consisting of the amino-terminal two-thirds of Sec10p directly
interacts with Sec15p, another exocyst component. Overexpression of
this domain displaces the full-length Sec10 from the exocyst complex,
resulting in a block in exocytosis and an accumulation of secretory
vesicles. The carboxy-terminal domain of Sec10p does not interact with
other members of the exocyst complex and expression of this domain does
not cause a secretory defect. Rather, this mutant results in the
formation of elongated cells, suggesting that the second domain of
Sec10p is required for morphogenesis, perhaps regulating the
reorientation of the secretory pathway from the tip of the emerging
daughter cell toward the mother–daughter connection during cell cycle
progression. The accurate targeting of secretory vesicles to distinct sites on the plasma membrane is necessary to achieve polarized growth and to establish specialized domains at the surface of eukaryotic cells. Members of a protein complex required for exocytosis, the exocyst, have been localized to regions of active secretion in the budding yeast Saccharomyces cerevisiae where they may function to specify sites on the plasma membrane for vesicle docking and fusion. In this study we have addressed the function of one member of the exocyst complex, Sec10p. We have identified two functional domains of Sec10p that act in a dominant-negative manner to inhibit cell growth upon overexpression. Phenotypic and biochemical analysis of the dominant-negative mutants points to a bifunctional role for Sec10p. One domain, consisting of the amino-terminal two-thirds of Sec10p directly interacts with Sec15p, another exocyst component. Overexpression of this domain displaces the full-length Sec10 from the exocyst complex, resulting in a block in exocytosis and an accumulation of secretory vesicles. The carboxy-terminal domain of Sec10p does not interact with other members of the exocyst complex and expression of this domain does not cause a secretory defect. Rather, this mutant results in the formation of elongated cells, suggesting that the second domain of Sec10p is required for morphogenesis, perhaps regulating the reorientation of the secretory pathway from the tip of the emerging daughter cell toward the mother-daughter connection during cell cycle progression. The accurate targeting of secretory vesicles to distinct sites on the plasma membrane is necessary to achieve polarized growth and to establish specialized domains at the surface of eukaryotic cells. Members of a protein complex required for exocytosis, the exocyst, have been localized to regions of active secretion in the budding yeastSaccharomyces cerevisiae where they may function to specify sites on the plasma membrane for vesicle docking and fusion. In this study we have addressed the function of one member of the exocyst complex, Sec10p. We have identified two functional domains of Sec10p that act in a dominant-negative manner to inhibit cell growth upon overexpression. Phenotypic and biochemical analysis of the dominant-negative mutants points to a bifunctional role for Sec10p. One domain, consisting of the amino-terminal two-thirds of Sec10p directly interacts with Sec15p, another exocyst component. Overexpression of this domain displaces the full-length Sec10 from the exocyst complex, resulting in a block in exocytosis and an accumulation of secretory vesicles. The carboxy-terminal domain of Sec10p does not interact with other members of the exocyst complex and expression of this domain does not cause a secretory defect. Rather, this mutant results in the formation of elongated cells, suggesting that the second domain of Sec10p is required for morphogenesis, perhaps regulating the reorientation of the secretory pathway from the tip of the emerging daughter cell toward the mother–daughter connection during cell cycle progression. |
Author | Roth, D Novick, P Guo, W |
AuthorAffiliation | Department of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06520-8002 |
AuthorAffiliation_xml | – name: Department of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06520-8002 |
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Notes | Corresponding Author Present address: Max-Planck Institute for Brain Research, Department of Neurochemistry, Deutschordenstr. 46, 60528 Frankfurt, Germany. |
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SubjectTerms | Alleles Fungal Proteins - biosynthesis Fungal Proteins - genetics Fungal Proteins - metabolism Genes, Dominant Genes, Fungal Genes, Lethal - genetics GTP-Binding Proteins - biosynthesis GTP-Binding Proteins - metabolism Mutagenesis, Site-Directed Myosin Heavy Chains Myosin Type V Myosins - metabolism Organelles - physiology Peptide Fragments - biosynthesis Peptide Fragments - genetics Peptide Fragments - metabolism Phenotype rab GTP-Binding Proteins Saccharomyces cerevisiae - cytology Saccharomyces cerevisiae - growth & development Saccharomyces cerevisiae - physiology Saccharomyces cerevisiae Proteins Vesicular Transport Proteins |
Title | Dominant negative alleles of SEC10 reveal distinct domains involved in secretion and morphogenesis in yeast |
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